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Conserved domains on  [gi|501527868|ref|WP_012534365|]
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MULTISPECIES: 3'(2'),5'-bisphosphate nucleotidase CysQ [Aliivibrio]

Protein Classification

FIG domain-containing protein( domain architecture ID 299)

FIG (FBPase/IMPase/glpX-like) domain-containing protein belongs to a superfamily of metal-dependent phosphatases with various substrates; such as fructose-1,6-bisphosphatase (both the major and the glpX-encoded variant), inositol-monophosphatases and inositol polyphosphatases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FIG super family cl00289
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 8-259 2.78e-134

FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.


The actual alignment was detected with superfamily member TIGR01331:

Pssm-ID: 469707 [Multi-domain]  Cd Length: 249  Bit Score: 379.10  E-value: 2.78e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868    8 LIPEVINIARASGQLILDIYEKGdFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWERYW 87
Cdd:TIGR01331   1 MLDDVIKIARAAGEEILPVYQKE-LAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   88 LVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKIPDmDESVRISTLKHEDEKQPIAIAI 167
Cdd:TIGR01331  80 LVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGD-GQALKAPIHVRPWPSGPLLVVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  168 SRRQDINNITRCMsSDWNYDLVPLGSAALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSYNER 247
Cdd:TIGR01331 159 SRSHAEEKTTEYL-ANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237

                         250
                  ....*....|..
gi 501527868  248 ESLENPNFIVLG 259
Cdd:TIGR01331 238 ESFRNPNFVALG 249
 
Name Accession Description Interval E-value
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 8-259 2.78e-134

3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 130398 [Multi-domain]  Cd Length: 249  Bit Score: 379.10  E-value: 2.78e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868    8 LIPEVINIARASGQLILDIYEKGdFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWERYW 87
Cdd:TIGR01331   1 MLDDVIKIARAAGEEILPVYQKE-LAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   88 LVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKIPDmDESVRISTLKHEDEKQPIAIAI 167
Cdd:TIGR01331  80 LVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGD-GQALKAPIHVRPWPSGPLLVVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  168 SRRQDINNITRCMsSDWNYDLVPLGSAALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSYNER 247
Cdd:TIGR01331 159 SRSHAEEKTTEYL-ANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237

                         250
                  ....*....|..
gi 501527868  248 ESLENPNFIVLG 259
Cdd:TIGR01331 238 ESFRNPNFVALG 249
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 5-260 6.96e-131

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 371.03  E-value: 6.96e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   5 LSHLIPEVINIARASGQLILDIYEKgDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWE 84
Cdd:COG1218    1 LEALLEAAIEIAREAGEAILEIYRA-DFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  85 RYWLVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKIPDMDESVRISTLKHEDEkQPIA 164
Cdd:COG1218   80 RFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGERQPIRVRDRPPA-EPLR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 165 IAISRRQDINNITRCMSSDWNYDLVPLGSaALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSY 244
Cdd:COG1218  159 VVASRSHRDEETEALLARLGVAELVSVGS-SLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRY 237

                        250
                 ....*....|....*.
gi 501527868 245 NERESLENPNFIVLGD 260
Cdd:COG1218  238 NKKEDLLNPGFIASGD 253
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 8-257 8.30e-107

CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).


Pssm-ID: 238816 [Multi-domain]  Cd Length: 242  Bit Score: 309.54  E-value: 8.30e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   8 LIPEVINIARASGQLILDIYeKGDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQraQWERYW 87
Cdd:cd01638    1 LLELLIRIAREAGDAILEVY-RGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRL--GWDRFW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  88 LVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKIpdmDESVRISTLKHEDEKQPIAIAI 167
Cdd:cd01638   78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKN---GRPGAVSLQARPPPLQPLRVVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 168 SRRQDINNITRCMSSDWNYDLVPLGSaALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSYNeR 247
Cdd:cd01638  155 SRSHPDEELEALLAALGVAEVVSIGS-SLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYN-R 232

                        250
                 ....*....|
gi 501527868 248 ESLENPNFIV 257
Cdd:cd01638  233 EDFLNPDFIA 242
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 8-257 1.18e-76

adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 233.05  E-value: 1.18e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   8 LIPEVINIARASGQLILDIYEkGD--FEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGiSLEQRAQWER 85
Cdd:PRK10931   1 MLEQICQLARNAGDAIMQVYD-GTkpLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPP-AWEVRQHWQR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  86 YWLVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKgAWKipdmDESVRISTLKHEDEKQPIaI 165
Cdd:PRK10931  79 YWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWK----EECGVRKQIQVRDARPPL-V 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 166 AISRRQDINNITRCMSSDWNYDLVPLGSaALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSYN 245
Cdd:PRK10931 153 VISRSHADAELKEYLQQLGEHQTTSIGS-SLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231

                        250
                 ....*....|..
gi 501527868 246 ERESLENPNFIV 257
Cdd:PRK10931 232 PRESFLNPGFRV 243
Inositol_P pfam00459
Inositol monophosphatase family;
5-254 5.20e-50

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 165.60  E-value: 5.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868    5 LSHLIPEVINIARASGQLILDIY--EKGDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQ 82
Cdd:pfam00459   2 LEEVLKVAVELAAKAGEILREAFsnKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   83 WERY-WLVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKipdmdESVRISTLKHEDEKQ 161
Cdd:pfam00459  82 DDGPtWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFL-----NGQPLPVSRAPPLSE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  162 PI---AIAISRRQDINN--ITRCMSSDWNYDLVP-LGSAALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRIL 235
Cdd:pfam00459 157 ALlvtLFGVSSRKDTSEasFLAKLLKLVRAPGVRrVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVT 236

                         250
                  ....*....|....*....
gi 501527868  236 STELEPLSYNERESLENPN 254
Cdd:pfam00459 237 DADGGPFDLLAGRVIAANP 255
 
Name Accession Description Interval E-value
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 8-259 2.78e-134

3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 130398 [Multi-domain]  Cd Length: 249  Bit Score: 379.10  E-value: 2.78e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868    8 LIPEVINIARASGQLILDIYEKGdFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWERYW 87
Cdd:TIGR01331   1 MLDDVIKIARAAGEEILPVYQKE-LAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   88 LVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKIPDmDESVRISTLKHEDEKQPIAIAI 167
Cdd:TIGR01331  80 LVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGD-GQALKAPIHVRPWPSGPLLVVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  168 SRRQDINNITRCMsSDWNYDLVPLGSAALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSYNER 247
Cdd:TIGR01331 159 SRSHAEEKTTEYL-ANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237

                         250
                  ....*....|..
gi 501527868  248 ESLENPNFIVLG 259
Cdd:TIGR01331 238 ESFRNPNFVALG 249
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 5-260 6.96e-131

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 371.03  E-value: 6.96e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   5 LSHLIPEVINIARASGQLILDIYEKgDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWE 84
Cdd:COG1218    1 LEALLEAAIEIAREAGEAILEIYRA-DFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  85 RYWLVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKIPDMDESVRISTLKHEDEkQPIA 164
Cdd:COG1218   80 RFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGERQPIRVRDRPPA-EPLR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 165 IAISRRQDINNITRCMSSDWNYDLVPLGSaALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSY 244
Cdd:COG1218  159 VVASRSHRDEETEALLARLGVAELVSVGS-SLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRY 237

                        250
                 ....*....|....*.
gi 501527868 245 NERESLENPNFIVLGD 260
Cdd:COG1218  238 NKKEDLLNPGFIASGD 253
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 8-257 8.30e-107

CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).


Pssm-ID: 238816 [Multi-domain]  Cd Length: 242  Bit Score: 309.54  E-value: 8.30e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   8 LIPEVINIARASGQLILDIYeKGDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQraQWERYW 87
Cdd:cd01638    1 LLELLIRIAREAGDAILEVY-RGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRL--GWDRFW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  88 LVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKIpdmDESVRISTLKHEDEKQPIAIAI 167
Cdd:cd01638   78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKN---GRPGAVSLQARPPPLQPLRVVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 168 SRRQDINNITRCMSSDWNYDLVPLGSaALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSYNeR 247
Cdd:cd01638  155 SRSHPDEELEALLAALGVAEVVSIGS-SLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYN-R 232

                        250
                 ....*....|
gi 501527868 248 ESLENPNFIV 257
Cdd:cd01638  233 EDFLNPDFIA 242
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 8-257 1.18e-76

adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 233.05  E-value: 1.18e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   8 LIPEVINIARASGQLILDIYEkGD--FEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGiSLEQRAQWER 85
Cdd:PRK10931   1 MLEQICQLARNAGDAIMQVYD-GTkpLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPP-AWEVRQHWQR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  86 YWLVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKgAWKipdmDESVRISTLKHEDEKQPIaI 165
Cdd:PRK10931  79 YWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWK----EECGVRKQIQVRDARPPL-V 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 166 AISRRQDINNITRCMSSDWNYDLVPLGSaALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRILSTELEPLSYN 245
Cdd:PRK10931 153 VISRSHADAELKEYLQQLGEHQTTSIGS-SLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231

                        250
                 ....*....|..
gi 501527868 246 ERESLENPNFIV 257
Cdd:PRK10931 232 PRESFLNPGFRV 243
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 12-247 9.40e-54

Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family [Carbohydrate transport and metabolism]; Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440251 [Multi-domain]  Cd Length: 255  Bit Score: 174.65  E-value: 9.40e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  12 VINIARASGQLILDIYEKGDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRaqwERYWLVDP 91
Cdd:COG0483    7 ALRAARAAGALILRRFRELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDS---GYVWVIDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  92 LDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKipdmdESVRISTLKHEDEKQPIaIAIS--- 168
Cdd:COG0483   84 IDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFL-----NGRRLRVSARTDLEDAL-VATGfpy 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 169 ---RRQDINNITRCMSSdwNYDLVPLGSAALKACLVAEGAVDCYLRLGpTGEWDTAATQCIVQEAGGRILSTELEPLSYN 245
Cdd:COG0483  158 lrdDREYLAALAALLPR--VRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPLDLG 234


                 ..
gi 501527868 246 ER 247
Cdd:COG0483  235 SG 236
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 12-250 4.15e-52

Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others.


Pssm-ID: 238815 [Multi-domain]  Cd Length: 238  Bit Score: 169.80  E-value: 4.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  12 VINIARASGQLILDIYEKGDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGisLEQRAQWERYWLVDP 91
Cdd:cd01637    4 ALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGG--SGNVSDGGRVWVIDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  92 LDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKipdmdESVRISTLKHEDEKQPIaIAISRRQ 171
Cdd:cd01637   82 IDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFL-----NGKKLPLSKDTPLNDAL-LSTNASM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 172 DINNITRCMSSdwnydLVP-------LGSAALKACLVAEGAVDCYLRLGPtGEWDTAATQCIVQEAGGRILSTELEPLSY 244
Cdd:cd01637  156 LRSNRAAVLAS-----LVNralgiriYGSAGLDLAYVAAGRLDAYLSSGL-NPWDYAAGALIVEEAGGIVTDLDGEPLDT 229


                 ....*.
gi 501527868 245 NERESL 250
Cdd:cd01637  230 LNRSGI 235
Inositol_P pfam00459
Inositol monophosphatase family;
5-254 5.20e-50

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 165.60  E-value: 5.20e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868    5 LSHLIPEVINIARASGQLILDIY--EKGDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQ 82
Cdd:pfam00459   2 LEEVLKVAVELAAKAGEILREAFsnKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   83 WERY-WLVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKipdmdESVRISTLKHEDEKQ 161
Cdd:pfam00459  82 DDGPtWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFL-----NGQPLPVSRAPPLSE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  162 PI---AIAISRRQDINN--ITRCMSSDWNYDLVP-LGSAALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRIL 235
Cdd:pfam00459 157 ALlvtLFGVSSRKDTSEasFLAKLLKLVRAPGVRrVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVT 236

                         250
                  ....*....|....*....
gi 501527868  236 STELEPLSYNERESLENPN 254
Cdd:pfam00459 237 DADGGPFDLLAGRVIAANP 255
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 12-247 5.95e-40

IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.


Pssm-ID: 238817 [Multi-domain]  Cd Length: 244  Bit Score: 138.82  E-value: 5.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  12 VINIARASGQLILDIYEKGDFEEFIKSDET-PVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRaqwERYWLVD 90
Cdd:cd01639    5 AIEAARKAGEILLEAYEKLGLNVEEKGSPVdLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTD---EPTWIID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  91 PLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKipdmdESVRISTLKHEDEKQ-------PI 163
Cdd:cd01639   82 PLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFL-----NGRRIRVSGRKELKDalvatgfPY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 164 AIAISRRQDINNI----------TRCMssdwnydlvplGSAALKACLVAEGAVDCY--LRLGPtgeWDTAATQCIVQEAG 231
Cdd:cd01639  157 DRGDNFDRYLNNFakllakavrgVRRL-----------GSAALDLAYVAAGRLDGYweRGLKP---WDVAAGALIVREAG 222

                        250
                 ....*....|....*.
gi 501527868 232 GRILSTELEPLSYNER 247
Cdd:cd01639  223 GLVTDFDGGPFDLMSG 238
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 37-257 4.03e-37

PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set.


Pssm-ID: 238775 [Multi-domain]  Cd Length: 274  Bit Score: 132.44  E-value: 4.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  37 KSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAgisleqrAQWERYWLVDPLDGTQEFIarSGD-FATIIALVENN 115
Cdd:cd01517   32 KSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS-------AALGRFWVLDPIDGTKGFL--RGDqFAVALALIEDG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 116 RPVMGVVYGPVS-------GVTYYAYEGKGAW---------------KIPDMDESVRISTLKHEDEKQPIAIAISRRQDI 173
Cdd:cd01517  103 EVVLGVIGCPNLplddgggGDLFSAVRGQGAWlrpldgsslqplsvrQLTNAARASFCESVESAHSSHRLQAAIKALGGT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 174 NNITRCMSsdwnydlvplgsaALKACLVAEGAVDCYLRLgPTGE------WDTAATQCIVQEAGGRILSTELEPLSY-NE 246
Cdd:cd01517  183 PQPVRLDS-------------QAKYAAVARGAADFYLRL-PLSMsyrekiWDHAAGVLIVEEAGGKVTDADGKPLDFgKG 248

                        250
                 ....*....|.
gi 501527868 247 RESLENPNFIV 257
Cdd:cd01517  249 RKLLNNGGLIA 259
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 12-259 2.34e-35

Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate inositol monophosphate or similar substrates.


Pssm-ID: 238821 [Multi-domain]  Cd Length: 242  Bit Score: 126.68  E-value: 2.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  12 VINIARASGQLILDiyekgDFEEFI----KSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGIslEQRAQWerYW 87
Cdd:cd01643    4 AEAIAQEAGDRALA-----DFGNSLsaetKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGI--FPSSGW--YW 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  88 LVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKipdMDESVRISTLKHEDEKQpIAIAI 167
Cdd:cd01643   75 VIDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFL---NGKPLALHPPLQLPDCN-VGFNR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 168 SRRQDINNITRCMSSDWNYDLVPLGSAALKACLVAEGAVDCYLRLGPTgEWDTAATQCIVQEAGGRILSTELEPLSYNER 247
Cdd:cd01643  151 SSRASARAVLRVILRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPK-IWDIAAAWVILREAGGSWTILDEEPAFLQTK 229

                        250
                 ....*....|..
gi 501527868 248 ESLENPNFIVLG 259
Cdd:cd01643  230 DYLSAGFPTLIA 241
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 15-234 1.33e-28

Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate fructose-1,6-bisphosphate, inositol monophospate, 3'-phosphoadenosine-5'-phosphate, or similar substrates.


Pssm-ID: 238819 [Multi-domain]  Cd Length: 248  Bit Score: 109.27  E-value: 1.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  15 IARASGQLILDIYEKGdFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWerywLVDPLDG 94
Cdd:cd01641    8 LADAAGQITLPYFRTR-LQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYVW----VLDPIDG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  95 TQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAW------------KIPDMDESVRIST----LKHED 158
Cdd:cd01641   83 TKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFlngaggrplrvrACADLAEAVLSTTdphfFTPGD 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501527868 159 EKQPIAIAISRRqdinnitrcmssdwnydLVPLGSAALKACLVAEGAVDCYLR--LGPtgeWDTAATQCIVQEAGGRI 234
Cdd:cd01641  163 RAAFERLARAVR-----------------LTRYGGDCYAYALVASGRVDLVVEagLKP---YDVAALIPIIEGAGGVI 220
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 11-234 4.74e-28

FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.


Pssm-ID: 238814 [Multi-domain]  Cd Length: 184  Bit Score: 105.94  E-value: 4.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  11 EVINIARASGQLILDIY--EKGDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWERYWL 88
Cdd:cd01636    3 ELCRVAKEAGLAILKAFgrELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTWV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  89 VDPLDGTQEFIARSGDFATIIALvennrpvmgvvygpvsGVTYYAYEgkgawkipdmdESVRISTLKHEdEKQPIAIAIS 168
Cdd:cd01636   83 IDPIDGTKNFINGLPFVAVVIAV----------------YVILILAE-----------PSHKRVDEKKA-ELQLLAVYRI 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501527868 169 RRqdinnitrcmssdwnydlvpLGSAALKACLVAEGAVDCYLRLGPTGE-WDTAATQCIVQEAGGRI 234
Cdd:cd01636  135 RI--------------------VGSAVAKMCLVALGLADIYYEPGGKRRaWDVAASAAIVREAGGIM 181
PLN02553 PLN02553
inositol-phosphate phosphatase
 13-235 3.74e-25

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 100.53  E-value: 3.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  13 INIARASGQLILD-IYEKGDFEEfiKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWERYWLVDP 91
Cdd:PLN02553  15 VDAAKAAGQIIRKgFYQTKHVEH--KGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELTDEPTWIVDP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  92 LDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKipdmdESVRISTLKHED-EKQPIAIAISRR 170
Cdd:PLN02553  93 LDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFL-----NGKPIKASSQSElGKALLATEVGTK 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501527868 171 QD----------INNITRCMSSdwnydLVPLGSAALKACLVAEGAVDCYLRLGPTGEWDTAATQCIVQEAGGRIL 235
Cdd:PLN02553 168 RDkatvdattnrINALLYKVRS-----LRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVF 237
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 13-234 2.46e-24

Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles.


Pssm-ID: 238773 [Multi-domain]  Cd Length: 257  Bit Score: 98.22  E-value: 2.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  13 INIARASGQLILDIYEKGDFEEFIK--SDETPVTSADLAAHKLIIEKLSQLTPdIPILSEEDAGISLEQRAQWerYWLVD 90
Cdd:cd01515    6 RNIAKEIEKAIKPLFGTEDASEVVKigADGTPTKLIDKVAEDAAIEILKKLGS-VNIVSEEIGVIDNGDEPEY--TVVLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  91 PLDGTQEFIARSGDFATIIALVENNR--PVMGVVYGPVSGVTYYAYEGKGAWKipdmdESVRISTLKHEDEKQPIAIAIS 168
Cdd:cd01515   83 PLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYL-----NGKRIKVSDFSSLKSISVSYYI 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501527868 169 RRQdinNITRCMSSDWNYDLVPL-GSAALKACLVAEGAVDCYLRLGPTGE-WDTAATQCIVQEAGGRI 234
Cdd:cd01515  158 YGK---NHDRTFKICRKVRRVRIfGSVALELCYVASGALDAFVDVRENLRlVDIAAGYLIAEEAGGIV 222
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
13-269 1.41e-23

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 96.13  E-value: 1.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  13 INIARASGQLILDIYEKGDFEEFIK--SDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEdAGISLEQRAQWERYwlVD 90
Cdd:PRK12676  11 DDMAKEVEKAIMPLFGTPDAGETVGmgADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEE-LGEIVGNGPEYTVV--LD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  91 PLDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAWKipdMDESVRISTLKhedEKQPIAIAIS-R 169
Cdd:PRK12676  88 PLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYL---NGKPIKVSKTS---ELNESAVSIYgY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 170 RQDINNITRCMSSDWNYDLvpLGSAALKACLVAEGAVDC------YLRlgPTgewDTAATQCIVQEAGGRILSTELEPLs 243
Cdd:PRK12676 162 RRGKERTVKLGRKVRRVRI--LGAIALELCYVASGRLDAfvdvrnYLR--VT---DIAAGKLICEEAGGIVTDEDGNEL- 233

                        250       260
                 ....*....|....*....|....*.
gi 501527868 244 YNERESLENPNFIVLGDENLpWNKIL 269
Cdd:PRK12676 234 KLPLNVTERTNLIAANGEEL-HKKIL 258
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 14-254 2.57e-23

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 96.24  E-value: 2.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  14 NIARA----SGQLILDIYEKGDfeefiKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEED------AGISLEQRAQW 83
Cdd:cd01640   14 GIARDvvkkGRLLILLVEGKTK-----EGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDnefenqEDESRDVDLDE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  84 ERYWL-----------------VDPLDGTQEFIARSGDFATI-IALVENNRPVMGVVYGPvsgvtYYAYEGKGAWKIPDM 145
Cdd:cd01640   89 EILEEscpspskdlpeedlgvwVDPLDATQEYTEGLLEYVTVlIGVAVKGKPIAGVIHQP-----FYEKTAGAGAWLGRT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 146 DESVR----ISTLKHEDEKQPIAIAISRRQDINNITRCMSSDWNYDLVPLGSAALKACLVAEGAVDCYLRL-GPTGEWDT 220
Cdd:cd01640  164 IWGLSglgaHSSDFKEREDAGKIIVSTSHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHStGGIKKWDI 243

                        250       260       270
                 ....*....|....*....|....*....|....
gi 501527868 221 AATQCIVQEAGGRILSTELEPLSYNERESLENPN 254
Cdd:cd01640  244 CAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKG 277
PRK10757 PRK10757
inositol-1-monophosphatase;
13-232 7.14e-21

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 89.10  E-value: 7.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  13 INIARASGQLILDIYEKGD-FEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRaqwERYWLVDP 91
Cdd:PRK10757   9 VRAARKAGNLIAKNYETPDaVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQ---DVQWVIDP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  92 LDGTQEFIARSGDFATIIALVENNRPVMGVVYGPVSGVTYYAYEGKGAW---------KIPDMDESVrIST---LKHEDE 159
Cdd:PRK10757  86 LDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQlngyrlrgsTARDLDGTI-LATgfpFKAKQH 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501527868 160 KQPIAIAISRRqdinnITRCMssdwnyDLVPLGSAALKACLVAEGAVDCYLRLGpTGEWDTAATQCIVQEAGG 232
Cdd:PRK10757 165 ATTYINIVGKL-----FTECA------DFRRTGSAALDLAYVAAGRVDGFFEIG-LKPWDFAAGELLVREAGG 225
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 37-257 8.26e-18

3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.


Pssm-ID: 273558 [Multi-domain]  Cd Length: 353  Bit Score: 81.83  E-value: 8.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   37 KSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAG----------------------------------ISLEQ--- 79
Cdd:TIGR01330  38 KDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDSSglseadftlgrvnelvnetlvyaknykkddqfplKSLEDvlq 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   80 ---RAQWE-----RYWLVDPLDGTQEFIaRSGDFATIIALVENNRPVMGVVYGP----------------VSGVTYYAYE 135
Cdd:TIGR01330 118 iidFGNYEggrkgRHWVLDPIDGTKGFL-RGDQYAVCLALIENGKVVLGVIGCPnlplssygaqnlkgseSKGCIFRAVR 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  136 GKGAWKIPdmdesvristlKHEDEKQPIAIAISRRQDINNITRCMS---SDWNYDL--------------VPLGSAAlKA 198
Cdd:TIGR01330 197 GSGAFMYS-----------LSSDAESPTKVHVSSVKDTKDAIFCEGvekGHSSHDEqtaianklgiskspLRLDSQA-KY 264

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501527868  199 CLVAEGAVDCYLRLGPTGE-----WDTAATQCIVQEAGGRILSTELEPLSYNERESLENPNFIV 257
Cdd:TIGR01330 265 AALARGDADVYLRLPIKLSyqekiWDHAAGNVIVEEAGGIVTDAMGKPLDFGKGRTLALDKGVI 328
PLN02737 PLN02737
inositol monophosphatase family protein
 5-250 7.47e-15

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 73.30  E-value: 7.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868   5 LSHLIPEVINIARASGQLILDIYEKGDFEEFiKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEdAGISLEqrAQWE 84
Cdd:PLN02737  76 AEELLAVAELAAKTGAEVVMEAVNKPRNISY-KGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEE-GGVIGD--SSSD 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  85 RYWLVDPLDGTQEFIARSGDFATIIALVENNRPVMGVVY----GPVSGVT--YYAYEGKGAW---------KIPDMDESV 149
Cdd:PLN02737 152 YLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVefvgGPMCWNTrtFSASAGGGAFcngqkihvsQTDKVERSL 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 150 RISTLKHEDEkQPIAIAISRRQDINNITRCMSSdwnydlvpLGSAALKACLVAEGAVDCY--LRLGPtgeWDTAATQCIV 227
Cdd:PLN02737 232 LVTGFGYEHD-DAWATNIELFKEFTDVSRGVRR--------LGAAAVDMCHVALGIVEAYweYRLKP---WDMAAGVLIV 299

                        250       260
                 ....*....|....*....|...
gi 501527868 228 QEAGGRILSTELEPLSYNERESL 250
Cdd:PLN02737 300 EEAGGTVTRMDGGKFSVFDRSVL 322
PLN02911 PLN02911
inositol-phosphate phosphatase
 14-126 2.80e-14

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 71.29  E-value: 2.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  14 NIARASGQLILDIYEKGdFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGISLEQRAQWerYWLVDPLD 93
Cdd:PLN02911  42 KLADAAGEVTRKYFRTK-FEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGSSDY--VWVLDPID 118

                         90       100       110
                 ....*....|....*....|....*....|...
gi 501527868  94 GTQEFIARSGDFATIIALVENNRPVMGVVYGPV 126
Cdd:PLN02911 119 GTKSFITGKPLFGTLIALLYKGKPVLGIIDQPV 151
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
27-250 8.57e-13

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 67.83  E-value: 8.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  27 YEKGDfeEFIK--SDETPVTSADLAAHKLIIEKLSQLTPDIpILSEEdAGISLEQRAQWERYWLVDPLDGTQEFIARSGD 104
Cdd:PRK14076  26 WEKAG--EVVKigADGTPTKRIDLIAENIAINSLEKFCSGI-LISEE-IGFKKIGKNKPEYIFVLDPIDGTYNALKDIPI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 105 FATIIAL-------------VENNRPV----MGVVYGPVSGVTYYAYEGKGAWkipdmdesvristLKHEDEKQPIAIAi 167
Cdd:PRK14076 102 YSASIAIakidgfdkkikefIGKNLTIndleVGVVKNIATGDTYYAEKGEGAY-------------LLKKGEKKKIEIS- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 168 srrqDINNITRCMSSDWNYDLVP----------------LGSAALKACLVAEGAVDCYLRLGPTGEW-DTAATQCIVQEA 230
Cdd:PRK14076 168 ----NISNLKDASIGLFAYGLSLdtlkfikdrkvrrirlFGSIALEMCYVASGALDAFINVNETTRLcDIAAGYVICKEA 243

                        250       260
                 ....*....|....*....|....
gi 501527868 231 GGRILSTELEP----LSYNERESL 250
Cdd:PRK14076 244 GGIITNKNGKPlnmkLDINEKTSV 267
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 12-263 2.13e-08

Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. These are Mg++ dependent phosphatases. Members in this family may have fructose-1,6-bisphosphatase and/or inositol-monophosphatase activity. Fructose-1,6-bisphosphatase catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway.


Pssm-ID: 238820 [Multi-domain]  Cd Length: 244  Bit Score: 53.61  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  12 VINIARASGQLILDIYEKGDFEEFIKSDETPVTSADLAAHKLIIEKLSQLTPDIPILSEEDAGIsleQRAQWERYWLVDP 91
Cdd:cd01642    5 LEKITKEIILLLNEKNRQGLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEI---RKGSGEYIAVLDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868  92 LDGTQEFIARSGDFATIIALVENNRPV-MGVVYGPVSGVTYYAYEGKGAWKIPDMDEsvRISTLKHEDEKQPIAIAISRR 170
Cdd:cd01642   82 LDGSTNYLSGIPFYSVSVALADPRSKVkAATLDNFVSGEGGLKVYSPPTRFSYISVP--KLGPPLVPEVPSKIGIYEGSS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501527868 171 QDINNItrCMSSDWNYDLVPLGSAALKACLVAEGAVDCYLRL-GPTGEWDTAATQCIVQEAGgrilstelepLSYNERES 249
Cdd:cd01642  160 RNPEKF--LLLSRNGLKFRSLGSAALELAYTCEGSFVLFLDLrGKLRNFDVAAALGACKRLG----------LHGDPSNL 227

                        250
                 ....*....|....
gi 501527868 250 LENPNFIVLGDENL 263
Cdd:cd01642  228 LLSRIKDKSIDEII 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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